Evidence map›Paper›PMID 25469942›Full record

ArticleBiomacromolecules2015

Stable, metastable, and kinetically trapped amyloid aggregate phases.

Tatiana Miti, Mentor Mulaj, Jeremy D Schmit, Martin Muschol

Abstract read
In one paragraph

Article in Biomacromolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed.

  1. Article
  2. Article
  3. Photolytic disruption of Alzheimer's amyloid AβCommunications chemistry · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022
    Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Tatiana MitiDepartment of Physics, University of South Florida , Tampa, Florida 33620, United States.
Mentor Mulaj
Jeremy D Schmit
Martin Muschol

Funding

Theoretical and computational modeling of amyloid aggregationR01GM107487 · NIGMS · KANSAS STATE UNIVERSITY · PI SCHMIT, JEREMY DAVID · 2014 to 2018
$1.4M
Does Charge Repulsion of Amyloids Regulate their Assembly Pathways and Toxicity?R15GM097723 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI MUSCHOL, MARTIN · 2012 to 2016
$773k
NIGMS NIH HHS R01 GM107487NIGMS NIH HHS R01GM107487NIGMS NIH HHS R15 GM097723NIGMS NIH HHS R15GM097723
6 · The paper itself

Abstract

Self-assembly of proteins into amyloid fibrils plays a key role in a multitude of human disorders that range from Alzheimer's disease to type II diabetes. Compact oligomeric species, observed early during amyloid formation, are reported as the molecular entities responsible for the toxic effects of amyloid self-assembly. However, the relation between early-stage oligomeric aggregates and late-stage rigid fibrils, which are the hallmark structure of amyloid plaques, has remained unclear. We show that these different structures occupy well-defined regions in a peculiar phase diagram. Lysozyme amyloid oligomers and their curvilinear fibrils only form after they cross a salt and protein concentration-dependent threshold. We also determine a boundary for the onset of amyloid oligomer precipitation. The oligomeric aggregates are structurally distinct from rigid fibrils and are metastable against nucleation and growth of rigid fibrils. These experimentally determined boundaries match well with colloidal model predictions that account for salt-modulated charge repulsion. The model also incorporates the metastable and kinetic character of oligomer phases. Similarities and differences of amyloid oligomer assembly to metastable liquid-liquid phase separation of proteins and to surfactant aggregation are discussed.

Indexed as

AmyloidHumansMicroscopy, Atomic ForceModels, ChemicalProtein ConformationProtein MultimerizationProtein StabilitySalinitySpectroscopy, Fourier Transform InfraredAmyloid

Identifiers

PMID25469942
PMCPMC4294590

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.